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Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks

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Science  09 Feb 2018:
Vol. 359, Issue 6376, pp. 698-701
DOI: 10.1126/science.aan6398

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Interactions of LARKS protein domains

More than 1500 human proteins contain long, disordered stretches of “low complexity”—strings of just a few of the 20 common amino acids. The functions of these low-complexity domains have been unclear. Hughes et al. present atomic-resolution structures that suggest that short segments of two such domains can bind weakly to each other by forming a pair of kinked β-sheets. Because aromatic amino acid side chains stabilize these interactions, the interacting motifs are termed LARKS, for low-complexity, aromatic-rich, kinked segments. Numerous proteins associated with membraneless organelles of biological cells contain low-complexity domains housing multiple LARKS.

Science, this issue p. 698